HIS1_THET2
ID HIS1_THET2 Reviewed; 206 AA.
AC P62381;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=ATP phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01018};
DE Short=ATP-PRT {ECO:0000255|HAMAP-Rule:MF_01018};
DE Short=ATP-PRTase {ECO:0000255|HAMAP-Rule:MF_01018};
DE EC=2.4.2.17 {ECO:0000255|HAMAP-Rule:MF_01018};
GN Name=hisG {ECO:0000255|HAMAP-Rule:MF_01018}; OrderedLocusNames=TT_C1866;
OS Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=262724;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX PubMed=15064768; DOI=10.1038/nbt956;
RA Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL Nat. Biotechnol. 22:547-553(2004).
CC -!- FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1-
CC diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial
CC role in the pathway because the rate of histidine biosynthesis seems to
CC be controlled primarily by regulation of HisG enzymatic activity.
CC {ECO:0000255|HAMAP-Rule:MF_01018}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = 5-phospho-
CC alpha-D-ribose 1-diphosphate + ATP; Xref=Rhea:RHEA:18473,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58017,
CC ChEBI:CHEBI:73183; EC=2.4.2.17; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01018};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC {ECO:0000255|HAMAP-Rule:MF_01018}.
CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC {ECO:0000255|HAMAP-Rule:MF_01018}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01018}.
CC -!- DOMAIN: Lacks the C-terminal regulatory region which is replaced by
CC HisZ.
CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. Short
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01018}.
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DR EMBL; AE017221; AAS82208.1; -; Genomic_DNA.
DR RefSeq; WP_011174220.1; NC_005835.1.
DR PDB; 1VE4; X-ray; 1.20 A; A=1-206.
DR PDBsum; 1VE4; -.
DR AlphaFoldDB; P62381; -.
DR SMR; P62381; -.
DR STRING; 262724.TT_C1866; -.
DR EnsemblBacteria; AAS82208; AAS82208; TT_C1866.
DR GeneID; 3168686; -.
DR KEGG; tth:TT_C1866; -.
DR eggNOG; COG0040; Bacteria.
DR HOGENOM; CLU_038115_2_0_0; -.
DR OMA; YVMMDYD; -.
DR OrthoDB; 1419568at2; -.
DR UniPathway; UPA00031; UER00006.
DR EvolutionaryTrace; P62381; -.
DR Proteomes; UP000000592; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd13595; PBP2_HisGs; 1.
DR HAMAP; MF_01018; HisG_Short; 1.
DR InterPro; IPR013820; ATP_PRibTrfase_cat.
DR InterPro; IPR018198; ATP_PRibTrfase_CS.
DR InterPro; IPR001348; ATP_PRibTrfase_HisG.
DR InterPro; IPR024893; ATP_PRibTrfase_HisG_short.
DR PANTHER; PTHR21403; PTHR21403; 1.
DR Pfam; PF01634; HisG; 1.
DR TIGRFAMs; TIGR00070; hisG; 1.
DR PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm;
KW Glycosyltransferase; Histidine biosynthesis; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..206
FT /note="ATP phosphoribosyltransferase"
FT /id="PRO_0000151945"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:1VE4"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:1VE4"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:1VE4"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:1VE4"
FT HELIX 57..62
FT /evidence="ECO:0007829|PDB:1VE4"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:1VE4"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:1VE4"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:1VE4"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:1VE4"
FT STRAND 110..114
FT /evidence="ECO:0007829|PDB:1VE4"
FT HELIX 116..125
FT /evidence="ECO:0007829|PDB:1VE4"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:1VE4"
FT HELIX 140..144
FT /evidence="ECO:0007829|PDB:1VE4"
FT STRAND 147..158
FT /evidence="ECO:0007829|PDB:1VE4"
FT HELIX 159..163
FT /evidence="ECO:0007829|PDB:1VE4"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:1VE4"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:1VE4"
FT HELIX 183..188
FT /evidence="ECO:0007829|PDB:1VE4"
FT HELIX 190..202
FT /evidence="ECO:0007829|PDB:1VE4"
SQ SEQUENCE 206 AA; 22381 MW; A9CC57D7E43069FE CRC64;
MRRFALTVAL PKGRMFREAY EVLKRAGLDL PEVEGERTLL HGKEGGVALL ELRNKDVPIY
VDLGIAEIGV VGKDVLLDSG RDLFEPVDLG FGACRLSLIR RPGDTGPIRR VATKYPNFTA
RLLKERGWAA DVVELSGNIE LAAVTGLADA VVDVVQTGAT LRAAGLVEVE VLAHSTARLV
VNRQALKLKR AVLKPLIQRL RELSGS
